Fluorescein 5'-Isothiocyanate-Modified Na^+, K^+-ATPase, at Lys-501 of the α-Chain, Accepts ATP Independent of Pyridoxal 5'-Diphospho-5'-Adenosine Modification at Lys-480^1
スポンサーリンク
概要
- 論文の詳細を見る
- Japanese Biochemical Societyの論文
- 1998-01-01
著者
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TANIGUCHI Kazuya
Biological Chemistry, Division of Chemistry, Faculty of Science, Hokkaido University
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Tsuda Takeo
Biological Chemistry Graduate School Of Science Hokkaido University
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Kaya Shunji
Biological Chemistry Graduate School Of Science Hokkaido University
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FUNATSU Hiroshi
Biological Chemistry, Graduate School of Science, Hokkaido University
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HAYASHI Utaro
Department of Biochemistry, School of Medicine, Kyorin University
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Hayashi Utaro
Department Of Biochemistry School Of Medicine Kyorin University
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Funatsu Hiroshi
Biological Chemistry Graduate School Of Science Hokkaido University
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Taniguchi Kazuya
Biological Chemistry Graduate School Of Science Hokkaido University
関連論文
- New Evidence for ATP Binding Induced Catalytic Subunit Interactions in Pig Kidney Na/K-ATPase
- Evidence for a Relationship between Activity and the Tetraprotomeric Assembly of Solubilized Pig Gastric H/K-ATPase
- The Oligomeric Nature of Na/K-Transport ATPase
- Direct Evidence for In Vivo Reversible Tyrosine Phosphorylation of the N-Terminal Domain of the H/K-ATPase α-Subunit in Mammalian Stomach Cells
- ATP-Induced Dynamic Fluorescence Changes of a N - [ p- (2-Benzimidazolyl)Phenyl] maleimide Probe at Cys^ in the α-Chain of Pig Stomach H^+, K^+-ATPase^1
- Fluorescein 5'-Isothiocyanate-Modified Na^+, K^+-ATPase, at Lys-501 of the α-Chain, Accepts ATP Independent of Pyridoxal 5'-Diphospho-5'-Adenosine Modification at Lys-480^1
- Direct Evidence for In Vivo Reversible Tyrosine Phosphorylation of the N-Terminal Domain of the H/K-ATPase .ALPHA.-Subunit in Mammalian Stomach Cells.